| Project/Area Number |
25840066
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Cell biology
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| Research Institution | Akita University |
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Principal Investigator |
TAMURA taku 秋田大学, 工学(系)研究科(研究院), 助教 (80363761)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2014: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | ALS / SOD1 / タンパク質凝集体 / 神経変性疾患 / アグリソーム / 脱凝集 / Myosin1b / アクチン / aggresomes / ミオシン / プロテアソーム |
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| Outline of Final Research Achievements |
SOD1 or superoxide dismutase 1 is one of the major incident of ALS (Amyotrophic Lateral Sclerosis). Genetically mutated SOD1 causes its protein aggregation specifically in neuron and eventually induces cell death. Detail in molecular mechanisms, however, in cell death induced by SOD1 aggregation. Biochemical and morphological analysis of interaction of aggregated SOD1 and actin and its motor protein Myosin1b was performed.
Overexpression of Myosin1b with mutant SOD1 in cultured cells revealed that mutated SOD1, which generally forms inclusion body (called aggressome), dispersed in whole cytoplasm. Furthermore, biochemical analysis indicated that ratio of aggregated SOD1 was decreased by the overexpression. These result suggest that Myosin1b participates the clearance of aggregated mutant SOD1 through intracellular degradation mechanism.
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